Process for removal of excess dye from printed or dyed fabric or yarn

ABSTRACT

The present invention provides a process for removal of excess dye from newly manufactured printed or dyed fabric or yarn, comprising treatment with a rinse liquor comprising at least one enzyme selected from the group consisting of enzymes exhibiting peroxidase activity or laccase activity, an oxidation agent, and at least one mediator selected from the group consisting of aliphatic, cyclo-aliphatic, heterocyclic or aromatic compounds containing the moiety &gt;N—OH, in particular 1-hydroxybenzotriazole.

CROSS-REFERENCE TO RELATED APPLICATIONS

[0001] This is a divisional application of application Ser. No.09/500,195 filed Feb. 8, 2000, which is a divisional application ofapplication Ser. No. 09/221,653 filed Dec. 23, 1998 and claims priorityof Danish application no. 1526/97 filed Dec. 23, 1997 and of U.S.provisional application No. 60/071,184 filed Jan. 12, 1998, the contentsof which are fully incorporated herein by reference.

BACKGROUND OF THE INVENTION

[0002] 1. Field of the Invention

[0003] The present invention relates to a novel method of removingexcess dye from newly printed or dyed fabric or yarn as well as a systemand a composition for use in the method.

[0004] 2 Description of Related Art

[0005] Printing and dyeing of textiles is carried out by applying dyesto the textile by any appropriate method for binding the dyestuff to thefibres in the textiles. Excess soluble dyestuff not bound to the fibresmust be removed after dyeing to ensure fastness of the dyed textiles andto prevent unwanted dye transfer during laundering of the textiles bythe consumer.

[0006] Generally, a large amount of water is required for completeremoval of excess dye. In a conventional process the printed or dyedtextile is first rinsed with cold water, then washed at high temperaturewith the addition of a suitable additive to decrease back-staining, likepoly(vinylpyrrolidone) (PVP). The process is repeated until asatisfactory amount of dyestuff (and thickeners) has been removed. PVPcan be added to reduce back-staining during rinsing, but this compounddoes not bleach the dye and is relatively expensive. Furthermore, thewaste liquor from a conventional process tends to be strongly coloredand may represent a disposal problem, which is not reduced by the use ofPVP.

[0007] WO 92/18687 discloses a method of bleaching excess dye fromprinted or dyed fabric by treating with a liquor containing an enzymeexhibiting peroxidase activity or oxidase activity, an O₂ or H₂O₂ sourceas applicable, and optionally an additional oxidizable substrate, suchas a metal ion, a halide ion or an organic compound, such as a phenol.

[0008] However, the concentrations of such additional substratesnecessary for enzymatically bleaching the excess dye in the rinse liquormay present a risk of bleaching the dyed textiles themselves.

[0009] Accordingly, it is an object of the present invention to providea method for removing or bleaching excess dye without bleaching the dyedtextile. This is achieved by a process for removal of excess dye fromnewly manufactured printed or dyed fabric or yarn comprising treatmentwith a rinse liquor comprising

[0010] at least one enzyme selected from the group consisting of enzymesexhibiting peroxidase activity or laccase activity,

[0011] an oxidation agent, and

[0012] at least one mediator selected from the group consisting ofaliphatic, cyclo-aliphatic, heterocyclic or aromatic compoundscontaining the moiety >N—OH, and

[0013] optionally additives.

[0014] In the present invention the term “mediator” means an additionaloxidizable substance improving the bleaching performance.

[0015] By suitable combination of mediator and enzyme it is possible toavoid bleaching of the dyed textile while bleaching dyes in solution,thereby reducing the amount of unbleached dye deposited on the fibresand thus increasing the wet fastness of the dyed or printed textile.

[0016] By this process it is furthermore possible to reduce the numberof rinsing steps and the temperature of the rinsing water in the rinsingsteps compared to the conventional processes, thereby saving energy andcosts.

[0017] Another object of the present invention is a system for removalof excess dye from newly manufactured printed or dyed fabric or yarn,which is a multi-component system comprising at least one enzymeselected from the group consisting of enzymes exhibiting peroxidaseactivity or laccase activity, an oxidation agent, and at least onemediator selected from the group consisting of aliphatic,cyclo-aliphatic, heterocyclic or aromatic compounds containing themoiety >N—OH, and optionally additives, such as rinsing additives.

[0018] The components of the system may be combined as a solution, aslurry or granulates depending on the specific enzymes and mediatorsselected.

[0019] A further object of the present invention is the use of thecomponents specified above for the preparation of a multi-componentsystem for removal of excess dye or print from newly manufactured fabricor yarn.

DETAILED DESCRIPTION OF THE INVENTION

[0020] Fabric or yarn

[0021] The process of the invention is applicable to all types oftextile materials, both natural fibres and synthetic fibres as well asblends thereof. Typical examples are cellulosic fibres (cotton andflax), modified cellulose fibres (e.g. acetate and triacetate), proteinfibres (e.g. wool and silk), polyamide fibres (e.g. nylon 6 and 6,6),polyester fibres (e.g. poly(ethylene terephthalate)) and acrylic fibres.

[0022] The process of the invention may be applied to dyed yarn, toknitted, woven or non-woven fabric, or to garments made from dyed and/orprinted fabric, especially garments made from differently coloredmaterial.

[0023] Printing method

[0024] The process of the invention is suited for excess dye bleachingafter any kind of textile printing. Examples of commonly used techniquesare printing on a Rotation film, a Rouleaux, a Flash film, or a Transferfilm device. After printing the dye is fixed on the textile by e.g.steaming or treatment with hot air.

[0025] Dyeing method

[0026] The process of the invention is suited for excess dye bleachingafter any kind of dyeing. The dyeing of textiles is for example carriedout by passing the fabric through a concentrated solution of dye,followed by storage of the wet fabric in a vapour tight enclosure topermit time for diffusion and reaction of the dye with the fabricsubstrate prior to rinsing off un-reacted dye. Alternatively, the dyemay be fixed by subsequent steaming of the textile prior to rinsing.

[0027] The process applies to any kind of dyes, such as reactive dyes.

[0028] Enzyme

[0029] Enzymes exhibiting peroxidase activity or laccase activity arethose which by using hydrogen peroxide or molecular oxygen, respectivelyare capable of oxidising a variety of compounds, such as phenols andaromatic amines.

[0030] According to the invention the concentration of enzyme is 0.005to 5 mg enzyme protein per l of rinse liquor, preferably, 0.02 to 2 mgenzyme protein per l of rinse liquor, more preferably 0.05 to 1 mgenzyme protein per l of rinse liquor. According to the liquor ratio,this may be translated to dosages of enzyme per kg of fabric, e.g. at aliquor ratio of 10:1, the most preferred enzyme dosage is from 0.5 to 10mg enzyme per kg of textile fabric.

[0031] Peroxidase activity exhibiting enzymes

[0032] An enzyme exhibiting peroxidase activity may be any peroxidasecomprised by the enzyme classification (EC 1.11.1.7), or ahaloperoxidase, such as a chloride peroxidase (EC 1.11.1.10) or anyfragment or synthetic or semisynthetic derivatives thereof exhibitingenzymatic activity (e.g. porphyrin ring systems or microperoxidases, cf.e.g. U.S. Pat. No. 4,077,768, EP 537 381, WO 91/05858 and WO 92/16634).Such enzymes are known from microbial, plant and animal origins.

[0033] Preferably, the peroxidase employed in the method of theinvention is producible by plants (e.g. horseradish or soybeanperoxidase), in particular soybean peroxidase, or by microorganisms,such as fungi (including filamentous fungi and yeasts) or bacteria.

[0034] Some preferred fungi include strains belonging to the subdivisionDeuteromycotina, class Hyphomycetes, e.g., Fusarium, Humicola,Tricoderma, Myrothecium, Verticillum, Arthromyces, Caldariomyces,Ulocladium, Embellisia, Cladosporium or Dreschlera, in particularFusarium oxysporum (DSM 2672), Humicola insolens, Trichoderma resii,Myrothecium verrucana (IFO 6113), Verticillum alboatrum, Verticillumdahlie, Adthromyces ramosus (FERM P-7754), Caldariomyces fumago,Ulocladium chartarum, Embellisia alli or Dreschlera halodes.

[0035] Other preferred fungi include strains belonging to thesubdivision Basidiomycotina, class Basidiomycetes, e.g. Coprinus,Phanerochaete, Coriolus or Trametes, in particular Coprinus cinereus f.microsporus (IFO 8371), Coprinus macrorhizus, Phanerochaetechrysosporium (e.g. NA-12) or Trametes (some classes previously calledPolyporus have been renamed to Trametes), e.g., T. versicolor (e.g. PR428-A).

[0036] Further preferred fungi include strains belonging to thesubdivision Zygomycotina, class Mycoraceae, e.g. Rhizopus or Mucor, inparticular Mucor hiemalis.

[0037] Some preferred bacteria include strains of the orderActinomycetales, e.g., Streptomyces spheroides (ATTC 23965),Streptomyces thermoviolaceus (IFO 12382) or Streptovefticillumvedticillium ssp. verticillium.

[0038] Other preferred bacteria include Bacillus pumilus (ATCC 12905),Bacillus stearothermophilus, Rhodobacter sphaeroides, Rhodomonaspalustri, Streptococcus lactis, Pseudomonas purrocinia (ATCC 15958) orPseudomonas fluorescens (NRRL B-11).

[0039] Further preferred bacteria include strains belonging toMyxococcus, e.g., M. virescens.

[0040] The peroxidase may furthermore be one which is producible by amethod comprising cultivating a host cell transformed with a recombinantDNA vector which carries a DNA sequence encoding said peroxidase as wellas DNA sequences encoding functions permitting the expression of the DNAsequence encoding the peroxidase, in a culture medium under conditionspermitting the expression of the peroxidase, and recovering theperoxidase from the culture.

[0041] Particularly, a recombinantly produced peroxidase is a peroxidasederived from a Coprinus sp., in particular C. macrorhizus or C. cinereusaccording to WO 92/16634, or a variant thereof.

[0042] In the context of this invention, peroxidase acting compoundscomprise peroxidase active fragments derived from cytochromes,hemoglobin or peroxidase enzymes, and synthetic or semisyntheticderivatives thereof, e.g. iron complexes of porphyrin or phthalocyanineand derivatives thereof.

[0043] Laccase and laccase related enzymes

[0044] In the context of this invention, the term “enzymes exhibitinglaccase activity” means laccases and laccase related enzymes, such asany laccase comprised by the enzyme classification (EC 1.10.3.2), anycatechol oxidase comprised by the enzyme classification (EC 1.10.3.1),any bilirubin oxidase comprised by the enzyme classification (EC1.3.3.5) or any monophenol monooxygenase comprised by the enzymeclassification (EC 1.14.99.1).

[0045] The laccases are known from microbial and plant origin. Themicrobial laccases may be derived from bacteria or fungi (includingfilamentous fungi and yeasts) and suitable examples include a laccasederivable from a strain of Aspergillus, Neurospora, e.g., N. crassa,Podospora, Botrytis, Collybia, Fomes, Lentinus, Pleurotus, Trametes,e.g., T. villosa and T. versicolor, Rhizoctonia, e.g., R. solani,Coprinus, e.g. C. plicatilis and C. cinereus, Psatyrella,Myceliophthora, e.g. M. thermophila, Schytalidium, Polyporus, e.g., P.pinsitus, Phlebia, e.g., P. radiata (WO 92/01046), or Coriolus, e.g., C.hirsutus (JP 2-238885), in particular a laccase derivable from a strainof Fomes, Trametes, Rhizoctonia, Coprinus, Myceliophthora, Schytalidium,or Polyporus.

[0046] The laccase or the laccase related enzyme may furthermore be onewhich is producible by a method comprising cultivating a host celltransformed with a recombinant DNA vector which carries a DNA sequenceencoding said laccase as well as DNA sequences encoding functionspermitting the expression of the DNA sequence encoding the laccase, in aculture medium under conditions permitting the expression of thelaccase, and recovering the laccase from the culture.

[0047] Oxidation agent

[0048] If the oxidizing enzyme requires a source of hydrogen peroxide,the source may be hydrogen peroxide or a hydrogen peroxide precursor forin situ production of hydrogen peroxide, e.g., a percarbonate or aperborate, a persulfate, such as a trioxo(peroxo)sulfate or aμ-peroxo-bis(trioxosulfate), a hydrogen peroxide-urea addition compound,a peroxycarboxylic acid or a salt thereof or a hydrogen peroxidegenerating enzyme system, e.g., an oxidase and a substrate for theoxidase, e.g. an amino acid oxidase and a suitable amino acid.

[0049] Hydrogen peroxide may be added at the beginning of or during theprocess, e.g., in a concentration corresponding to 0.01-50 mM H₂O₂,preferably 0.1 to 5 mM.

[0050] If the oxidizing enzyme requires molecular oxygen, molecularoxygen from the atmosphere will usually be present in sufficientquantity. Otherwise pure O₂ may be led to the rinse liquor, or an O₂generating enzymatic system, e.g. a system based on hydrogen peroxideand a catalase, may be added.

[0051] Mediator

[0052] According to the invention at least one mediator selected fromthe group consisting of aliphatic, cyclo-aliphatic, heterocyclic oraromatic compounds containing the moiety >N—OH is added to the rinseliquor. In a preferred embodiment of the invention the mediator is acompound of formula I:

[0053] wherein R¹, R², R³, R⁴ are individually selected from the groupconsisting of hydrogen, halogen, hydroxy, formyl, carboxy and salts andesters thereof, amino, nitro, C₁-C₁₂ alkyl, C₁-C₆ alkoxy,carbonyl(C₁-C₁₂ alkyl), aryl, in particular phenyl, sulfo,aminosulfonyl, carbamoyl, phosphono, phosphonooxy, and salts and estersthereof, wherein the R¹, R², R³, R⁴ may be substituted with R⁵, whereinR⁵ represents hydrogen, halogen, hydroxy, formyl, carboxy and salts andesters thereof, amino, nitro, C₁-C₁₂ alkyl, C₁-C₆ alkoxy,carbonyl(C₁-C₁₂ alkyl), aryl, in particular phenyl, sulfo,aminosulfonyl, carbamoyl, phosphono, phosphonooxy, and salts and estersthereof, [X] is a group from (—N═N—), (—N═CR⁶—)_(m), (—CR⁶═N—)_(m),(—CR⁷═CR⁸—)_(m), and m is 1 or 2.

[0054] In a more preferred embodiment of the invention the mediator is acompound of formula

[0055] wherein R¹, R², R³, R⁴ are individually selected from the groupconsisting of hydrogen, halogen, hydroxy, formyl, carboxy and salts andesters thereof, amino, nitro, C₁-C₁₂ alkyl, C₁-C₆ alkoxy,carbonyl(C₁-C₁₂ alkyl), aryl, in particular phenyl, sulfo,aminosulfonyl, carbamoyl, phosphono, phosphonooxy, and salts and estersthereof, wherein the R¹, R², R³, R⁴ may be substituted with R⁵, whereinR⁵ represents hydrogen, halogen, hydroxy, formyl, carboxy and salts andesters thereof, amino, nitro, C₁-C₁₂ alkyl, C₁-C₆ alkoxy,carbonyl(C₁-C₁₂ alkyl), aryl, in particular phenyl, sulfo,aminosulfonyl, carbamoyl, phosphono, phosphonooxy, and salts and estersthereof.

[0056] The mediator may also be a salt or an ester of formula I or II.

[0057] Further preferred mediators are oxoderivatives and N-hydroxyderivatives of heterocyclic compounds and oximes of oxo- andformyl-derivatives of heterocyclic compounds, said heterocycliccompounds including five-membered nitrogen-containing heterocycles, inparticular pyrrol, pyrazole and imidazole and their hydrogenatedcounterparts (e.g. pyrrolidine) as well as triazoles, such as1,2,4-triazole; six-membered nitrogen-containing heterocycles, inparticular mono-, di- and triazinanes (such as piperidine andpiperazine), morpholine and their unsaturated counterparts (e.g.pyridine and pyrimidine); and condensed heterocycles containing theabove heterocycles as substructures, e.g. indole, benzothiazole,quinoline and benzoazepine.

[0058] Examples of preferred mediators from these classes of compoundsare pyridine aldoximes; N-hydroxypyrrolidinediones such asN-hydroxysuccinimide and N-hydroxyphthalimide;3,4-dihydro-3-hydroxybenzo[1,2,3]triazine-4-one; formaldoxime trimer(N,N′,N″-trihydroxy-1,3,5-triazinane); and violuric acid (1,3-diazinane-2,4,5,6-tetrone-5-oxime).

[0059] Still further mediators which may be applied in the inventioninclude oximes of oxo- and formyl-derivatives of aromatic compounds,such as benzoquinone dioxime and salicylaldoxime (2-hydroxybenzaldehydeoxime), and N-hydroxyamides and N-hydroxyanilides, such asN-hydroxyacetanilide.

[0060] Preferred mediators are selected from the group consisting of1-hydroxybenzotriazole; 1-hydroxybenzotriazole hydrate;1-hydroxybenzotriazole sodium salt; 1-hydroxybenzotriazole potassiumsalt; 1-hydroxybenzotriazole lithium salt; 1-hydroxybenzotriazoleammonium salt; 1-hydroxybenzotriazole calcium salt;1-hydroxybenzotriazole magnesium salt; and1-hydroxybenzotriazole-6-sulphonic acid.

[0061] A particularly preferred mediator is 1-hydroxybenzotriazole.

[0062] All the specifications of N-hydroxy compounds above areunderstood to include tautomeric forms such as N-oxides wheneverrelevant.

[0063] Usually, the concentration of mediator in the rinse liquor isfrom 0.1 μM to 50 mM, preferably 1 μM to 1 mM, more preferably 10 μM to0.5 mM.

[0064] Additives

[0065] The rinse liquor may comprise further additives, such assurfactants and/or water conditioning agents.

[0066] Multi-component system

[0067] In order to carry out the process described above amulti-component system is added to the rinse liquor in at least one ofthe rinsing steps.

[0068] The components of the multi-component system may individually bein one of several product forms, such as a slurry, a solution or agranulate.

[0069] In one embodiment of the invention two components are mixed inthe represented form, such as a co-granulate, a solution or a slurrycomprising enzyme and mediator.

[0070] In cases of co-granulates, the co-granulate may comprise at leastone enzyme and at least one mediator. Another example of a co-granulateis a granulate comprising at least two different enzymes and optionallyat least one mediator.

[0071] In a further embodiment the system is a mixture of granulateswherein the component(s) in one granulate is(are) enzyme(s) and thecomponent(s) in another granulate is(are) mediator(s).

[0072] According to the present invention a preferred multi-componentsystem comprises at least one enzyme selected from the group consistingof enzymes exhibiting peroxidase activity or laccase activity,optionally an oxidation agent, and at least one mediator selected fromthe group consisting of aliphatic, cyclo-aliphatic, heterocyclic oraromatic compounds containing the moiety >N—OH as described above, andoptionally additives, such as rinsing additives.

[0073] The enzymes exhibiting peroxidase activity or laccase activityare preferably as described above.

[0074] The system may comprise an oxidation agent, but in cases wherethe enzyme is an enzyme exhibiting laccase activity, molecular oxygenfrom the atmosphere is normally sufficient, and the system used will notcomprise an oxidation agent. However, when the enzymes used requireaddition of an oxidation agent those are as described above. In allcases wherein a H₂O₂ source is the oxidation agent the enzyme andoxidation agent may not be mixed before use.

[0075] The mediator is as described above, in a preferred embodiment themediator is selected from the group consisting of oxoderivatives andN-hydroxy derivatives of heterocyclic compounds and oximes of oxo- andformyl-derivatives of heterocyclic compounds, said heterocycliccompounds including five-membered nitrogen-containing heterocycles, inparticular pyrrol, pyrazole and imidazole and their hydrogenatedcounterparts (e.g. pyrrolidine) as well as triazoles, such as1,2,4-triazole; six-membered nitrogen-containing heterocycles, inparticular mono-, di- and triazinanes (such as piperidine andpiperazine), morpholine and their unsaturated counterparts (e.g.pyridine and pyrimidine); and condensed heterocycles containing theabove heterocycles as substructures, e.g. indole, benzothiazole,quinoline and benzoazepine.

[0076] Examples of preferred mediators from these classes of compoundsare pyridine aldoximes; N-hydroxypyrrolidinediones such asN-hydroxysuccinimide and N-hydroxyphthalimide;3,4-dihydro-3-hydroxybenzo[1,2,3]triazine-4-one; formaldoxime trimer(N,N′,N″-trihydroxy-1,3,5-triazinane); and violuric acid(1,3-diazinane-2,4,5,6-tetrone-5-oxime).

[0077] Still further mediators which may be applied in the inventioninclude oximes of oxo- and formyl-derivatives of aromatic compounds,such as benzoquinone dioxime and salicylaldoxime (2-hydroxybenzaldehydeoxime), and N-hydroxyamides and N-hydroxyanilides, such asN-hydroxyacetanilide.

[0078] A particularly preferred mediator is 1-hydroxybenzotriazole.

[0079] All the specifications of N-hydroxy compounds above areunderstood to include tautomeric forms such as N-oxides wheneverrelevant.

[0080] A further aspect of the present invention is the use ofcomponents comprising

[0081] at least one enzyme selected from the group consisting of enzymesexhibiting peroxidase activity or laccase activity,

[0082] optionally an oxidation agent, and

[0083] at least one mediator selected from the group consisting ofaliphatic, cyclo-aliphatic, heterocyclic or aromatic compoundscontaining the moiety >N—OH, and

[0084] optionally additives

[0085] for the preparation of a multi-component system for removal ofexcess dye or print from newly manufactured fabric or yarn.

[0086] Process conditions

[0087] The removal of excess dye, according to the invention, maycomprise rinsing with rinse liquor in 2 to 6 rinsing steps, morepreferred in 2 to 5 rinsing steps, even more preferred in 2 to 4 rinsingsteps, in particular in 3 to 4 rinsing steps. The amount of rinsingsteps is dependent on the concentration of the mediator and of theconcentration of the peroxidase.

[0088] The multi-component system as defined according to this inventionmay be used in any of the rinsing steps performed, however it ispreferably added in one of the last rinsing steps, in particular in thethird or fourth rinsing step.

[0089] The process may be run in batch mode or continuous mode. Theprocess may be applied on a winch, a beck, a jet dyer, an open-widthwashing machine, a J or U box, a steamer, or any other equipmentavailable suitable for a rinsing process.

[0090] The process conditions must be chosen according to thecharacteristics of the enzyme in question. The temperature at therinsing step comprising a multi-component system as defined above ispreferably ranging from 40° C. to 80° C., such as from 50° C. to 70° C.,and pH is typically in the range of 5.5-9.5, such as 6.5-9.

[0091] Fatness

[0092] Fastness (wet, crock, light, etc.) may be measured by variousmethods as known in the art. Wet fastness may be measured as describedbelow. Colorfastness to crocking, which is designed to determine theamount of color transferred from the surface of colored materials toother surfaces by rubbing, may be measured according to AATCC TestMethod 8-1996. Colorfastness to light, in which samples of the materialto be tested and the agreed upon comparison standard(s) are exposedsimultaneously to a light source under specified conditions, may bemeasured according to AATCC Test Method 16-1993.

[0093] Wet fastness

[0094] The multi-component system as defined above is added to therinsing liquor to prevent re-deposition of solubilized excess dye bybleaching it in solution.

[0095] The wet fastness or water fastness reflects the degree to whichthis has successfully been achieved.

[0096] In the present invention the wet fastness is measured by thestandard method (DIN 54 006). Briefly, the method comprises soaking adyed fabric and pressing it together with swatches of white fabric.After separate drying of the fabrics, the swatches are evaluated forstaining.

[0097] The degree of wet fastness is indicated on a scale, the highernumber the better wet fastness. 1 means very low wet fastness, whereas 5means very high wet fastness.

[0098] Color measurement (Example 5)

[0099] A Gretag-Mecbath Color Eye 3100 was used according to themanufacturer's instructions to evaluate the chromaticity using thechange in the color space coordinates L*a*b* (CIELAB-system), where asusual:

[0100] L* gives the change in white/black on a scale from 0 to 100, anda decrease in L* means an increase in black color (decrease in whitecolor) and an increase in L* means an increase in white color (decreasein black color).

[0101] a* gives the change in red/green, and a decrease in a* means anincrease in green color (decrease in red color), and an increase in a*means an increase in red color (decrease in green color).

[0102] b* gives the change in blue/yellow, and a decrease in b* means anincrease in blue color (decrease in yellow color), and an increase in b*means an increase in yellow color (decrease in blue color) (Vide WO96/12846 NOVO).

[0103] The Gretag-Macbeth Color Eye 3100 was operated in the L*a*b*color space. The light source was D65 standard light. The software usedfor evaluation was Optiview Quality Control 1.7c. The observation anglewas 10°. The instrument was calibrated using a Macbeth calibration plate(white). Each result was an average of 10 measurements. Fabric rinsedwithout enzyme and mediator was measured and the coordinates L*a*b* werecalculated and entered as a reference. The coordinates of the sampleswere then for each of L*, a*, b* calculated as the difference (A) of theaverage of the measurements on each swatch from the reference value.

[0104] The present invention is further illustrated in the followingexamples which are not in any

Example 1 Reactive dyeing of cotton fabric followed by an enzymaticrinsing process

[0105] Knitted, bleached 100% cooton was dyed in a Mathis jet-dryer(laboratory scale jet dyeing machine) under the following conditions:way intended to limit the scope of the invention as claimed. Water:softened water, 10 l/kg of fabric Temperature: 50° C. Dyestuff: 4%LEVAFIX Scarlet E-2GA (Reactive Red 123) Na₂SO₄: 50 g/l Na₂CO₃: 4 g/lNaOH (32%): 2 ml/l LEVEGAL RL: 1.0 g/l (levelling agent) ERKANTOL NR:1.0 g/l (wetting agent) PERSOFTAL L: 1.0 g/l (crease-preventing agent)RESPUMIT S: 1.0 g/l (antifoaming agent)

[0106] The dyeing process started at 50° C. by addition of dyestuff,Na₂SO₄, LEVEGAL RL, ERKANTOL NR, PERSOFTAL L and RESPUMIT S. Na₂CO₃ wasadded 30 minutes after start and NaOH 60 minutes after start. During thewhole process the temperature was held at 50° C.

[0107] 60 minutes after addition of NaOH the dyeing process was stoppedby draining off the dyeing liquor, whereafter the rinsing process wasstarted.

[0108] The rinsing process was carried out as follows:

[0109] First rinsing step:

[0110] Addition of fresh softened water; 10 l/kg fabric.

[0111] Rinsing 10 minutes at 40° C.

[0112] Draining the rinsing liquor.

[0113] Second rinsing step:

[0114] Addition of fresh softened water; 10 l/kg fabric.

[0115] Addition of 10 ml/l of acetic acid (6 % solution in water)

[0116] Rinsing 20 minutes at 95° C.

[0117] Draining the rinsing liquor.

[0118] Third rinsing step:

[0119] Addition of fresh softened water; 10 l/kg fabric.

[0120] Addition of 5.0 ml/l of potassium phosphate buffer (1.0 M,pH=7.0)

[0121] Rinsing 40 minutes at 60° C.

[0122] Addition of 0.8 mg/l Peroxidase SP502, 55 mg/l (0.4 mM) HOBT and39 mg/l (0.4 mM) H₂O₂ (35 % solution in water)

[0123] Rinsing 10 minutes at 60° C.

[0124] Draining the rinsing liquor.

[0125] SP502 was a liquid preparation of recombinant Coprinus cinereusperoxidase supplied by Novo Nordisk A/S (produced as described in WO92/16634). HOBT was 1-hydroxybenzotriazole ex Sigma.

[0126] The fabric was squeezed and dried. The wet fastness wasdetermined according to DIN 54 006. The degree of fastness was found tobe 3 (adjacent fabric cotton).

EXAMPLE 2 (For Comparison)

[0127] Conventional 3 step rinsing process

[0128] The dyeing process was carried out as described in Example 1. Therinsing steps were carried out as follows.

[0129] First rinsing step:

[0130] Addition of fresh softened water; 10 l/kg fabric.

[0131] Rinsing 10 minutes at 40° C.

[0132] Draining the rinsing liquor.

[0133] Second rinsing step:

[0134] Addition of fresh softened water; 10 l/kg fabric.

[0135] Rinsing 20 minutes at 95° C.

[0136] Draining the rinsing liquor.

[0137] Third rinsing step:

[0138] Addition of fresh softened water; 10 l/kg fabric.

[0139] Rinsing 10 minutes at 80° C.

[0140] Draining the rinsing liquor.

[0141] The fabric was squeezed and dried. The wet fastness wasdetermined according to DIN 54 006. The degree of fastness was found tobe 2 (adjacent fabric cotton).

EXAMPLE 3 (For Comparison)

[0142] Conventional 4 step rinsing process

[0143] The dyeing process was carried out as described in Example 1. Therinsing steps were carried out as follows.

[0144] First rinsing step:

[0145] Addition of fresh softened water; 10 l/kg fabric.

[0146] Rinsing 10 minutes at 40° C.

[0147] Draining the rinsing liquor.

[0148] Second rinsing step:

[0149] Addition of fresh softened water; 10 l/kg fabric.

[0150] Rinsing 10 minutes at 70° C.

[0151] Draining the rinsing liquor.

[0152] Third rinsing step:

[0153] Addition of fresh softened water; 10 l/kg fabric.

[0154] Rinsing 20 minutes at 95° C.

[0155] Draining the rinsing liquor.

[0156] Fourth rinsing step:

[0157] Addition of fresh softened water; 10 l/kg fabric.

[0158] Rinsing 10 minutes at 40° C.

[0159] Draining the rinsing liquor.

[0160] The fabric was squeezed and dried. The wet fastness wasdetermined according to DIN 54 006. The degree of fastness was found tobe 2-3 (adjacent fabric cotton).

EXAMPLE 4 (For Comparison)

[0161] Conventional 6 step rinsing process

[0162] The dyeing process was carried out as described in Example 1. Therinsing steps were carried out as follows.

[0163] First rinsing step:

[0164] Addition of fresh softened water; 10 l/kg fabric.

[0165] Rinsing 10 minutes at 40° C.

[0166] Draining the rinsing liquor.

[0167] Second rinsing step:

[0168] Addition of fresh softened water; 10 l/kg fabric.

[0169] Rinsing 10 minutes at 70° C.

[0170] Draining the rinsing liquor.

[0171] Third rinsing step:

[0172] Addition of fresh softened water; 10 l/kg fabric.

[0173] Rinsing 10 minutes at 70° C.

[0174] Draining the rinsing liquor.

[0175] Fourth rinsing step:

[0176] Addition of fresh softened water; 10 l/kg fabric.

[0177] Rinsing 20 minutes at 95° C.

[0178] Draining the rinsing liquor.

[0179] Fifth rinsing step:

[0180] Addition of fresh softened water; 10 l/kg fabric.

[0181] Rinsing 10 minutes at 70° C.

[0182] Draining the rinsing liquor.

[0183] Sixth rinsing step:

[0184] Addition of fresh softened water; 10 l/kg fabric.

[0185] Rinsing 10 minutes at 40° C.

[0186] Draining the rinsing liquor.

[0187] The fabric was squeezed and dried. The wet fastness wasdetermined according to DIN 54006. The degree of fastness was found tobe 3 (adjacent fabric cotton).

[0188] Conclusion: The wet fastness 3 (corresponding to the conventional6 step rinsing process) was also obtained by the process according tothe invention (see Example 1), whereby a substantial amount of rinsingsteps can be avoided (saving water and energy and process time).

EXAMPLE 5

[0189] Reactive dyeing of cotton fabric followed by enzymatic rinsingprocesses using two different mediators

[0190] Knitted, bleached 100% cotton was dyed in a Mathis jet-dyer(laboratory scale jet dyeing machine) at the following conditions:Water: softened water, 10 l/kg of fabric Dyestuff: 1% Remazol Yellow RR1% Remazol Red RR 1% Remazol Blue RR Na₂SO₄: 70 g/l Na₂CO₃: 5 g/l NaOH(32% in water): 3 ml/l LEVEGAL RL: 1.0 g/l (levelling agent) ERKANTOLNR: 1.0 g/l (wetting agent) PERSOFTAL L: 1.0 g/l (crease-preventingagent)

[0191] The dyeing process started at 30° C. by addition of Na₂CO₃, NaOH(1 ml/l), Na₂SO₄, LEVEGAL RL, ERKANTOL NR, PERSOFTAL L. The dyestuffswere added 15 minutes after start. 30 minutes after start thetemperature was increased up to 50° C. within 20 minutes. 30 minutesafter reaching 50° C. the remaining NaOH (2 ml/l) was added. 45 minutesafter the addition of NaOH (2 ml/l) the dyeing process was finished bydraining off the dyeing liquor, whereafter the rinsing process wasstarted.

[0192] The following rinsing process was carried out for each mediator(1-hydroxybenzotriazole (according to the invention); and methylsyringate (comparison)):

[0193] First rinsing step:

[0194] Addition of fresh softened water; 10 l/kg fabric.

[0195] Rinsing 10 minutes at 40° C.

[0196] Draining the rinsing liquor.

[0197] Second rinsing step:

[0198] Addition of fresh softened water; 10 l/kg fabric.

[0199] Addition of 10 ml/l of acetic acid (6% solution in water)

[0200] Rinsing 20 minutes at 95° C.

[0201] Draining the rinsing liquor.

[0202] Third rinsing step:

[0203] Addition of fresh softened water; 10 l/kg fabric.

[0204] Addition of 5.0 ml/l of potassium phosphate buffer (1.0 M,pH=7.0)

[0205] Rinsing 40 minutes at 60° C.

[0206] Addition of 0.8 mg/l Peroxidase SP502, 0.4 mM mediator and 39mg/l (0.4 mM) H₂O₂ (35% solution in water)

[0207] Rinsing 10 minutes at 60° C.

[0208] Draining the rinsing liquor.

[0209] SP502 was a liquid preparation of recombinant Coprinus cinereusperoxidase supplied by Novo Nordisk A/S.

[0210] The fabric was squeezed and dried. A color measurement wasperformed using a color measuring instrument (Gretag-Macbeth Color Eye3100) as described above.

[0211] Results:

[0212] Mediator: 1-hydroxybenzotriazole

[0213] ΔL*=0.756

[0214] Δa*=0.045

[0215] Δb*=0.022

[0216] Mediator: Methyl syringate

[0217] ΔL*=3.142

[0218] Δa*=0.134

[0219] Δb*=0.834

[0220] Conclusion: It can be seen that methyl syringate has asignificant and undesired influence on the chromaticity of the fabric.The positive Δb* of 0.834 indicates a very strong and not acceptableincrease in yellow color whereas a Δb* of 0.022 which is found for1-hydroxybenzotriazole is negligible and not visible. It is seen thatalso ΔL* and Δa* are significantly smaller in the treatment according tothe invention than in the comparison treatment.

EXAMPLE 6

[0221] Enzymatic bleaching of soluble dyes

[0222] The dyes tested were Reactive Black 5 (Remazol Black B), ReactiveRed 198 (Remazol Red RB), Reactive Blue 220(Remazol Brilliant Blue BB),Reactive Blue 21 (Remazol Turquoise Blue G), and Reactive Orange 107(Remazol Golden Yellow RNL), all ex Dystar. All dyes were dissolved in a0.5 mM sodium phosphate buffer (pH 7.0) to an initial absorbance ofapproximately 0.4 at the wavelength λmax of maximum absorbance withinthe visible range. The solutions were then placed in a thermostatedquartz cell in a HP 8453 diode array spectrophotometer, the threecomponents of the enzymatic oxidation system were added (CiP to 0.2mg/l, HOBT to 100 μM, hydrogen peroxide to 200 μM), and the absorbanceABS(λmax) at λmax monitored over time. The degree of bleaching at 5 min,i.e. the decrease in ABSλkmax) over 5 min divided by ABS(λmax) at t=0,is shown below, measured at three temperatures. Degree of bleaching at 5min (%): Reactive Black 5 (λmax = 596 nm): 79 (60° C.); 82 (70° C.); 72(80° C.); Reactive Red 198 (λmax = 517 nm): 97 (60° C.); 100 (70° C.);88 (80° C.); Reactive Blue 220 (λmax = 608 nm): 100 (60° C.); 98 (70°C.); 30 (80° C.); Reactive Blue 21 (λmax = 663 nm): 100 (60° C.); 88(70° C.); 61(80° C.); Reactive Orange 107 (λmax = 408 nm): 90 (60° C.);67 (70° C.); 36 (80° C.).

[0223] This example demonstrates that one of the preferred mediatorsaccording to the invention, HOBT (1-hydroxybenzotriazole), combined withCoprinus cinereus peroxidase (CiP) and hydrogen peroxide, provides highdegrees of bleaching of soluble dyes in short time with a range ofreactive dyes.

1. A process for removal of excess dye from newly manufactured printedor dyed fabric or yarn, comprising treatment with a rinse liquorcomprising (a) at least one enzyme exhibiting peroxidase activity orlaccase activity, (b) an oxidation agent, (c) at least one mediatorselected from the group consisting of aliphatic, cyclo-aliphatic,heterocyclic or aromatic compounds containing the moiety >N—OH, and (d)optionally additives.
 2. A process of claim 1 , wherein the enzyme is alaccase (EC 1.10.3.2), catechol oxidase (EC 1.10.3.1), bilirubin oxidase(EC 1.3.3.5), peroxidase (EC 1.11.1.7), or haloperoxidase, such as achloride peroxidase (EC 1.11.1.10) or any fragment derived therefromexhibiting enzymatic activity or synthetic or semisynthetic derivativesthereof.
 3. A process of claim 2 , wherein the peroxidase is derivedfrom a strain of Coprinus or from soybean.
 4. A process of claim 2 ,wherein the laccase is derived from a strain of Fomes, Trametes,Rhizoctonia, Coprinus, Myceliophthora, Schytalidium, or Polyporus.
 5. Aprocess of any of the preceding claims, wherein the amount of enzyme is0.005 to 5 mg enzyme protein per l of rinse liquor, preferably, 0.02 to2 mg enzyme protein per l of rinse liquor, more preferably 0.05 to 1 mgenzyme protein per l of rinse liquor.
 6. A process of any of thepreceding claims, wherein the oxidation agent is a H₂O₂ source.
 7. Aprocess of claim 6 , wherein the H₂O₂ source is hydrogen peroxide, aperborate, a percarbonate, a persulfate, a peroxycarboxylic acid or asalt thereof, or an enzymatic system capable of generating hydrogenperoxide.
 8. A process of claim 7 , wherein the concentration of H₂O₂ isfrom 0.01 to 50 mM, preferably 0.1 to 5 mM.
 9. A process of any of theclaims 1-5, wherein the oxidation agent is a O₂ source.
 10. A process ofclaim 9 , wherein the O₂ source is air, pure O₂, or an O₂ generatingenzymatic system.
 11. A process of any of the preceding claims, whereinthe mediator is a compound of formula I:

wherein R¹, R², R³, R⁴ are individually selected from the groupconsisting of hydrogen, halogen, hydroxy, formyl, carboxy and salts andesters thereof, amino, nitro, C₁-C₁₂ alkyl, C₁-C₆ alkoxy,carbonyl(C₁-C₁₂ alkyl), aryl, in particular phenyl, sulfo,aminosulfonyl, carbamoyl, phosphono, phosphonooxy, and salts and estersthereof, wherein the R¹, R², R³, R⁴ may be substituted with R⁵, whereinR⁵ represents hydrogen, halogen, hydroxy, formyl, carboxy and salts andesters thereof, amino, nitro, C₁-C₁₂ alkyl, C₁-C₆ alkoxy,carbonyl(C₁-C₁₂ alkyl), aryl, in particular phenyl, sulfo,aminosulfonyl, carbamoyl, phosphono, phosphonooxy, and salts and estersthereof, [X] is a group from (—N═N—), (—N═CR⁶—)_(m), (—CR⁶═N—)_(m),(—CR⁷═CR⁸—)_(m), and m is 1 or2.
 12. A process of claim 11 , wherein themediator is a compound of formula II:

wherein R¹, R², R³, R⁴ are as defined in claim 11 or a salt or an esterthereof.
 13. A process of claim 12 , wherein the mediator is1-hydroxybenzotriazole.
 14. A process of any of the preceding claims,wherein the concentration of mediator in the rinse liquor is from 0.1 μMto 50 mM, preferably 1 μM to 1 mM, more preferably 10 μM to 0.5 mM. 15.A process of any of the preceding claims, wherein the additives aresurfactants and/or water conditioning agents.
 16. A process of any ofthe preceding claims, wherein the dye or print is a reactive dye.
 17. Asystem for removal of excess dye from newly manufactured printed or dyedfabric or yarn, which is a multi-component system comprising (a) atleast one enzyme exhibiting peroxidase activity or laccase activity, (b)optionally an oxidation agent, (c) at least one mediator selected fromthe group consisting of aliphatic, cyclo-aliphatic, heterocyclic oraromatic compounds containing the moiety >N—OH, and (d) optionallyadditives.
 18. A system of claim 17 , wherein the enzyme is a laccase(EC 1.10.3.2), catechol oxidase (EC 1.10.3.1), bilirubin oxidase (EC1.3.3.5), peroxidase (EC 1.11.1.7), or haloperoxidase, such as achloride peroxidase (EC 1.11.1.10) or any fragment derived therefromexhibiting enzymatic activity or synthetic or semisynthetic derivatives.19. A system of claim 18 , wherein the peroxidase is derived from astrain of Coprinus or from soybean.
 20. A system of claim 18 , whereinthe laccase is derived from a strain of Fomes, Trametes, Rhizoctonia,Coprinus, Myceliophthora, Schytalidium, or Polyporus.
 21. A system ofany of the claims 17-20, wherein the oxidation agent is a H₂O₂ source.22. A system of claim 21 , wherein the H₂O₂ source is hydrogen peroxide,a perborate, a percarbonate, a persulfate, a peroxycarboxylic acid or asalt thereof, or an enzymatic system capable of generating hydrogenperoxide.
 23. A system of claim 22 , wherein the concentration of H₂O₂is from 0.01 to 50 mM, preferably 0.1 to 5 mM.
 24. A system of any ofthe claims 17-20, wherein the oxidation agent is an O₂ source.
 25. Asystem of claim 24 , wherein the O₂ source is air, pure O₂, or an O₂generating enzymatic system.
 26. A system of any of the claims 17-25,wherein the mediator is a compound of formula I:

wherein R¹, R², R³, R⁴ are individually selected from the groupconsisting of hydrogen, halogen, hydroxy, formyl, carboxy and salts andesters thereof, amino, nitro, C₁-C₁₂ alkyl, C₁-C₆ alkoxy,carbonyl(C₁-C₁₂ alkyl), aryl, in particular phenyl, sulfo,aminosulfonyl, carbamoyl, phosphono, phosphonooxy, and salts and estersthereof, wherein the R¹, R², R³, R⁴ may be substituted with R⁵, whereinR⁵ represents hydrogen, halogen, hydroxy, formyl, carboxy and salts andesters thereof, amino, nitro, C₁-C₁₂ alkyl, C₁-C₆ alkoxy,carbonyl(C₁-C₁₂ alkyl), aryl, in particular phenyl, sulfo,aminosulfonyl, carbamoyl, phosphono, phosphonooxy, and salts and estersthereof, [X] is a group from (—N═N—), (—N═CR⁶—)_(m), (—CR⁶═N—)_(m),(—CR⁷═CR⁸—)_(m), and m is 1 or
 2. 27. A system of claim 26 , wherein themediator is a compound of formula II:

wherein R¹, R², R³, R⁴ are as defined in claim 26 or a salt or esterthereof.
 28. A system of claim 27 , wherein the mediator is1-hydroxybenzotriazole.
 29. A system of any of the claims 17-28, whereinone component is a solution comprising the enzyme(s) and themediator(s).
 30. A system of any of the claims 17-28, wherein onecomponent is a slurry comprising the enzyme(s) and the mediator(s). 31.A system of any of the claims 17-28, wherein one component is agranulate comprising the enzyme(s) and the mediator(s).
 32. A system ofclaims 17-28, wherein one component is a granulate comprising theenzyme(s) and another component is a granulate comprising themediator(s).
 33. Use of components comprising (a) at least one enzymeexhibiting peroxidase activity or laccase activity, (b) optionally anoxidation agent, (c) at least one mediator selected from the groupconsisting of aliphatic, cyclo-aliphatic, heterocyclic or aromaticcompounds containing the moiety >N—OH, and (d) optionally additives forthe preparation of a multi-component system for removal of excess dye orprint from newly manufactured fabric or yarn.
 34. A process for removalof excess dye from newly manufactured printed or dyed fabric or yarn,comprising treatment with a rinse liquor comprising (a) at least oneenzyme exhibiting peroxidase activity or laccase activity, (b) anoxidation agent, and (c) N-hydroxyacetanilide.
 35. The process of claim34 , wherein the rinse liquor further comprises additives.
 36. Theprocess of claim 34 , wherein the enzyme is a laccase (EC 1.10.3.2),catechol oxidase (EC 1.10.3.1), bilirubin oxidase (EC 1.3.3.5), aperoxidase (EC 1.11.1.7), or haloperoxidase
 37. The process of claim 36, wherein the enzyme is a chloride peroxidase (EC 1.11.1.10).
 38. Theprocess of claim 36 , wherein the peroxidase is derived from a strain ofCoprinus or from soybean.
 39. The process of claim 36 , wherein thelaccase is derived from a strain of Fomes, Trametes, Rhizoctonia,Coprinus, Myceliophthora, Schytalidium, or Polyporus.
 40. The process ofclaim 34 , wherein the amount of enzyme is 0.005 to 5 mg enzyme proteinper l of rinse liquor.
 41. The process of claim 34 , wherein theoxidation agent is a H₂O₂ source.
 42. The process of claim 34 , whereinthe oxidation agent is an O₂ source.
 43. The process of claim 34 ,wherein the concentration of N-hydroxyacetanilide in the rinse liquor isfrom 0.1 μM to 50 mM.
 44. The process of claim 43 , wherein theconcentration of N-hydroxyacetanilide in the rinse liquor is from 1 μMto 1 mM.
 45. The process of claim 44 , wherein the concentration ofN-hydroxyacetanilide in the rinse liquor is from 10 μM to 0.5 mM. 46.The process of claim 35 , wherein the additives are surfactants and/orwater conditioning agents.
 47. The process of claim 34 , wherein the dyeor print is a reactive dye.
 48. A system for removal of excess dye fromnewly manufactured printed or dyed fabric or yarn, which is amulti-component system comprising (a) at least one enzyme exhibitingperoxidase activity or laccase activity, (b) optionally an oxidationagent, (c) N-hydroxyacetanilide, and (d) optionally additives.
 49. Thesystem of claim 48 , wherein the enzyme is a laccase (EC 1.10.3.2), acatechol oxidase (EC 1.10.3.1), a bilirubin oxidase (EC 1.3.3.5), aperoxidase (EC 1.11.1.7), or a haloperoxidase.
 50. The system of claim49 , wherein the enzyme is a chloride peroxidase (EC 1.11.1.10).
 51. Thesystem of claim 49 , wherein the peroxidase is derived from a strain ofCoprinus or sI from soybean.
 52. The system of claim 49 , wherein thelaccase is derived from a strain of Fomes, Trametes, Rhizoctonia,Coprinus, Myceliophthora, Schytalidium, or Polyporus.
 53. The system ofclaim 48 , wherein the oxidation agent is a H₂O₂ source.
 54. The systemof claim 48 , wherein the oxidation agent is an O₂ source.
 55. Thesystem of claim 48 , wherein one component is a solution comprising theenzyme(s) and the mediator(s).
 56. The system of claim 48 , wherein onecomponent is a slurry comprising the enzyme(s) and the mediator(s). 57.The system of claim 48 , wherein one component is a granulate comprisingthe enzyme(s) and the mediator(s).
 58. The system of claim 48 , whereinone component is a granulate comprising the enzyme(s) and anothercomponent is a granulate comprising the mediator(s).